1pag | pdb_00001pag

THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN

spinqualitylabelsall models 1pag, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pag is a 2 chain structure with sequence from American pokeweed. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RIP1_PHYAM] Inhibits viral infection of plants, and protein synthesis in vitro. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The pokeweed antiviral protein (PAP), isolated from the leaves of Phytolacca americana, is one of a family of plant and bacterial ribosome-inhibiting proteins (RIPs) which act as specific N-glycosidases on rRNA. Here we report the three-dimensional structure of PAP determined to 2.5 A resolution by X-ray crystallography. After 14 rounds of refinement, the R factor is 0.17 for 5.0 to 2.5 A data. The protein is homologous with the A chain of ricin and exhibits a very similar folding pattern. The positions of key active site residues are also similar. We also report the 2.8 A structure of PAP complexed with a substrate analog, formycin 5'-monophosphate. As seen previously in ricin, the formycin ring is stacked between invariant tyrosines 72 and 123. Arg179 bonds to N-3 which is thought to be important in catalysis. The 2.5 A structure of pokeweed antiviral protein.,Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD J Mol Biol. 1993 Oct 20;233(4):705-15. PMID:8411176 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome inactivating protein

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